ID   LYSC2_PIG               Reviewed;         146 AA.
AC   P12068;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Lysozyme C-2;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8728388; DOI=10.1006/mpev.1996.0025;
RA   Yu M., Irwin D.M.;
RT   "Evolution of stomach lysozyme: the pig lysozyme gene.";
RL   Mol. Phylogenet. Evol. 5:298-308(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 19-146.
RC   TISSUE=Stomach;
RX   PubMed=2504928; DOI=10.1007/bf02602933;
RA   Jolles J., Jolles P., Bowman B.H., Prager E.M., Stewart C.-B., Wilson A.C.;
RT   "Episodic evolution in the stomach lysozymes of ruminants.";
RL   J. Mol. Evol. 28:528-535(1989).
CC   -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC       tissues and body fluids are associated with the monocyte-macrophage
CC       system and enhance the activity of immunoagents.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC       transglycosylation; it shows also a slight esterase activity. It acts
CC       rapidly on both peptide-substituted and unsubstituted peptidoglycan,
CC       and slowly on chitin oligosaccharides.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U28757; AAB16862.1; -; Genomic_DNA.
DR   RefSeq; NP_999557.2; NM_214392.2.
DR   AlphaFoldDB; P12068; -.
DR   SMR; P12068; -.
DR   STRING; 9823.ENSSSCP00000042981; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PaxDb; 9823-ENSSSCP00000000522; -.
DR   PeptideAtlas; P12068; -.
DR   GeneID; 100157211; -.
DR   KEGG; ssc:100157211; -.
DR   CTD; 4069; -.
DR   eggNOG; ENOG502S1S1; Eukaryota.
DR   HOGENOM; CLU_111620_0_1_1; -.
DR   InParanoid; P12068; -.
DR   OrthoDB; 5344399at2759; -.
DR   TreeFam; TF324882; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd16897; LYZ_C; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   PANTHER; PTHR11407:SF28; LYSOZYME C; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
DR   Genevisible; P12068; SS.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Digestion; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:2504928"
FT   CHAIN           19..146
FT                   /note="Lysozyme C-2"
FT                   /id="PRO_0000018479"
FT   DOMAIN          19..146
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        24..144
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        48..132
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        81..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        93..111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ   SEQUENCE   146 AA;  16484 MW;  C2986F5CAAAF49F4 CRC64;
     MKTLLVLALL LLSVSVQAKV YDRCEFARIL KKSGMDGYRG VSLANWVCLA KWESDFNTKA
     INHNVGSTDY GIFQINSRYW CNDGKTPKAV NACHISCKVL LDDDLSQDIE CAKRVVRDPL
     GVKAWVAWRA HCQNKDVSQY IRGCKL
//